6AAG

Crystal structure of budding yeast Atg8 complexed with the helical AIM of Hfl1.

Summary for 6AAG

• Entry DOI: 10.2210/pdb6aag/pdb
• Descriptor: Transmembrane protein 184 homolog YKR051W,Autophagy-related protein 8 (2 entities in total)
• Functional Keywords: vacuole autophagy, membrane protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 7
• Total formula weight: 113339.55

Authors

Yamasaki, A.,Noda, N.N. (deposition date: 2018-07-18, release date: 2018-12-12, Last modification date: 2023-11-22)

Primary citation

Liu, X.M.,Yamasaki, A.,Du, X.M.,Coffman, V.C.,Ohsumi, Y.,Nakatogawa, H.,Wu, J.Q.,Noda, N.N.,Du, L.L.
Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein
Elife, 7:-, 2018

PubMed Abstract: The ubiquitin-like protein Atg8, in its lipidated form, plays central roles in autophagy. Yet, remarkably, Atg8 also carries out lipidation-independent functions in non-autophagic processes. How Atg8 performs its moonlighting roles is unclear. Here we report that in the fission yeast and the budding yeast , the lipidation-independent roles of Atg8 in maintaining normal morphology and functions of the vacuole require its interaction with a vacuole membrane protein Hfl1 (homolog of human TMEM184 proteins). Crystal structures revealed that the Atg8-Hfl1 interaction is not mediated by the typical Atg8-family-interacting motif (AIM) that forms an intermolecular β-sheet with Atg8. Instead, the Atg8-binding regions in Hfl1 proteins adopt a helical conformation, thus representing a new type of AIMs (termed helical AIMs here). These results deepen our understanding of both the functional versatility of Atg8 and the mechanistic diversity of Atg8 binding.

PubMed: 30451685
DOI: 10.7554/eLife.41237

Experimental method

X-RAY DIFFRACTION (2.445 Å)